Abstract
The cyanogen bromide (CNBr) fragments of the two link proteins (LP) were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The observed apparent molecular weight difference between LP1 (Mr = 44,500) and LP2 (Mr = 48,500) was the reflect of a molecular weight difference between their NH2-terminal CNBr fragments (Mr = 19,000 and 24,000 for LP1 and LP2, respectively). The latter are glycosylated contrary to the COOH-terminal parts of the molecules. Fluorhydric acid/pyridine treatment suggests that LP1 and LP2 have a protein core of identical size. They differ from their common tryptic fragment (T-G200-3 fraction) by the presence of an additional short peptide. The latter was highly glycosylated in LP2 but not in LP1. Deglycosylation together with CNBr treatment corroborates the hypothesis that LP1 and LP2 possess a similar protein core.
Highlights
The cyanogen bromide (CNBr) fragments of the two link proteins (LP) were examined by sodium dodecyl sulfate-polyacrylamidegel electrophoresis
The only separation procedure of the twolink proteinsisstillthat described in 1978 by Bonnet etal. [4]; theirmolecular weights determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresisare 44,500 and 48,500 (4, 5 )
The two link proteins appear chemically closely related according to the following different criteria:( a ) their aminoacid compositions are quite identical [4,5,6]; ( b )they both appeared unsensitive to automated Edman degradation [7]; (c) they have bneoetn clearly immunologically distinguished [8]; ( d ) they behaved identically on isoelectrofocusing gels [9]; ( e ) upon cyanogen bromide treatment, theygave rise, under reducing conditions, to a major fragment [7,8,9,10] whose NH2-terminalsequence has been determined [7];( f ) upon tryptic[11]and Staphylococcus
Summary
The cyanogen bromide (CNBr) fragments of the two link proteins (LP) were examined by sodium dodecyl sulfate-polyacrylamidegel electrophoresis. Fluorhydric acidlpyridine treatment suggests that LP1 and LP2 have a protein core of identical size They differ from their common tryptic fragment (T-G200-3 fraction) by the presence of an additional short peptide. The two link proteins appear chemically closely related according to the following different criteria:( a ) their aminoacid compositions are quite identical [4,5,6]; ( b )they both appeared unsensitive to automated Edman degradation [7]; (c) they have bneoetn clearly immunologically distinguished [8]; ( d ) they behaved identically on isoelectrofocusing gels [9]; ( e ) upon cyanogen bromide treatment, theygave rise, under reducing conditions, to a major fragment [7,8,9,10] whose NH2-terminalsequence has been determined [7];( f ) upon tryptic[11]and Staphylococcus et de la Recherche Medicale (Unite U-116), the Centre National de laRechercheScientifique(ER102),andtheFondationpour la Recherche M6dicale FranGaise. Inthisreport,thedetailedstudy of the cyanogen bromidefragmentstogether with deglycosylation experiments demonstrates the structural identityof the protein cores of the two link proteins andallows the localization of their sugarmoieties
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